AT1B1_RAT
ID AT1B1_RAT Reviewed; 304 AA.
AC P07340; Q63062;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-1;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-1;
GN Name=Atp1b1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=3025616; DOI=10.1128/mcb.6.11.3884-3890.1986;
RA Mercer R.W., Schneider J.W., Savitz A., Emanuel J.R., Benz E.J. Jr.,
RA Levenson R.;
RT "Rat-brain Na,K-ATPase beta-chain gene: primary structure, tissue-specific
RT expression, and amplification in ouabain-resistant HeLa C+ cells.";
RL Mol. Cell. Biol. 6:3884-3890(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3031033; DOI=10.1016/s0021-9258(18)61282-7;
RA Young R.M., Shull G.E., Lingrel J.B.;
RT "Multiple mRNAs from rat kidney and brain encode a single Na+,K+-ATPase
RT beta subunit protein.";
RL J. Biol. Chem. 262:4905-4910(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=1314096; DOI=10.1016/0167-4781(92)90449-a;
RA Liu B., Gick G.;
RT "Characterization of the 5' flanking region of the rat Na+/K(+)-ATPase beta
RT 1 subunit gene.";
RL Biochim. Biophys. Acta 1130:336-338(1992).
RN [5]
RP PROTEIN SEQUENCE OF 15-21; 72-85; 97-107; 205-217 AND 279-291, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP INTERACTION WITH ATP12A, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=14749213; DOI=10.1152/ajpcell.00393.2003;
RA Pestov N.B., Korneenko T.V., Radkov R., Zhao H., Shakhparonov M.I.,
RA Modyanov N.N.;
RT "Identification of the beta-subunit for nongastric H-K-ATPase in rat
RT anterior prostate.";
RL Am. J. Physiol. 286:C1229-C1237(2004).
RN [7]
RP INTERACTION WITH FXYD3.
RX PubMed=15743908; DOI=10.1091/mbc.e04-10-0878;
RA Crambert G., Li C., Claeys D., Geering K.;
RT "FXYD3 (Mat-8), a new regulator of Na,K-ATPase.";
RL Mol. Biol. Cell 16:2363-2371(2005).
RN [8]
RP FUNCTION IN ADHESION.
RX PubMed=22328500; DOI=10.1242/jcs.100149;
RA Tokhtaeva E., Sachs G., Sun H., Dada L.A., Sznajder J.I., Vagin O.;
RT "Identification of the amino acid region involved in the intercellular
RT interaction between the beta1 subunits of Na+/K+ -ATPase.";
RL J. Cell Sci. 125:1605-1616(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP INTERACTION WITH FXYD1.
RX PubMed=23532852; DOI=10.1074/jbc.m113.460956;
RA Wypijewski K.J., Howie J., Reilly L., Tulloch L.B., Aughton K.L.,
RA McLatchie L.M., Shattock M.J., Calaghan S.C., Fuller W.;
RT "A separate pool of cardiac phospholemman that does not regulate or
RT associate with the sodium pump: multimers of phospholemman in ventricular
RT muscle.";
RL J. Biol. Chem. 288:13808-13820(2013).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The beta subunit
CC regulates, through assembly of alpha/beta heterodimers, the number of
CC sodium pumps transported to the plasma membrane (PubMed:22328500).
CC Plays a role in innate immunity by enhancing virus-triggered induction
CC of interferons (IFNs) and interferon stimulated genes (ISGs).
CC Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well
CC as the phosphorylation of TAK1 and TBK1 (By similarity).
CC {ECO:0000250|UniProtKB:P05026, ECO:0000269|PubMed:22328500}.
CC -!- FUNCTION: Involved in cell adhesion and establishing epithelial cell
CC polarity. {ECO:0000269|PubMed:22328500}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit (By similarity). Interacts with catalytic
CC subunit ATP12A (PubMed:14749213). Interacts with regulatory subunit
CC FXYD1 (PubMed:23532852). Interacts with regulatory subunit FXYD3
CC (PubMed:15743908). Interacts with NKAIN1, NKAIN2 and NKAIN4 (By
CC similarity). Interacts with MLC1 (By similarity). Part of a complex
CC containing MLC1, TRPV4, AQP4 and HEPACAM (By similarity). Interacts
CC with KIRREL3 (By similarity). Interacts with OBSCN (via protein kinase
CC domain 1) (By similarity). Interacts with TRAF3 and TRAF6 (By
CC similarity). {ECO:0000250|UniProtKB:P05026,
CC ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:14749213,
CC ECO:0000269|PubMed:15743908, ECO:0000269|PubMed:23532852}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:14749213}; Single-pass type II membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P14094}. Note=Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes. Localizes in long
CC striations at the level of Z and M lines.
CC {ECO:0000250|UniProtKB:P14094}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, liver, testes and anterior
CC prostate (at protein level). {ECO:0000269|PubMed:14749213}.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- PTM: Glutathionylated. N-glycosylated (PubMed:14749213).
CC {ECO:0000250|UniProtKB:P14094, ECO:0000269|PubMed:14749213}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; M14137; AAA40781.1; -; mRNA.
DR EMBL; J02701; AAA40780.1; -; mRNA.
DR EMBL; BC078902; AAH78902.1; -; mRNA.
DR EMBL; X63375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A25082; PWRTNB.
DR RefSeq; NP_037245.2; NM_013113.2.
DR AlphaFoldDB; P07340; -.
DR SMR; P07340; -.
DR BioGRID; 247679; 5.
DR IntAct; P07340; 7.
DR MINT; P07340; -.
DR STRING; 10116.ENSRNOP00000003932; -.
DR BindingDB; P07340; -.
DR ChEMBL; CHEMBL4106147; -.
DR ChEMBL; CHEMBL4106148; -.
DR ChEMBL; CHEMBL4106149; -.
DR ChEMBL; CHEMBL4106165; -.
DR GlyGen; P07340; 3 sites, 46 N-linked glycans (2 sites).
DR iPTMnet; P07340; -.
DR PhosphoSitePlus; P07340; -.
DR SwissPalm; P07340; -.
DR jPOST; P07340; -.
DR PaxDb; P07340; -.
DR PRIDE; P07340; -.
DR GeneID; 25650; -.
DR KEGG; rno:25650; -.
DR UCSC; RGD:2170; rat.
DR CTD; 481; -.
DR RGD; 2170; Atp1b1.
DR VEuPathDB; HostDB:ENSRNOG00000002934; -.
DR eggNOG; KOG3927; Eukaryota.
DR HOGENOM; CLU_057702_2_0_1; -.
DR InParanoid; P07340; -.
DR OMA; ECKAYGQ; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P07340; -.
DR TreeFam; TF314618; -.
DR Reactome; R-RNO-210991; Basigin interactions.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-936837; Ion transport by P-type ATPases.
DR SABIO-RK; P07340; -.
DR PRO; PR:P07340; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002934; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; P07340; baseline and differential.
DR Genevisible; P07340; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0005901; C:caveola; IDA:RGD.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0031090; C:organelle membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:ARUK-UCL.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0001671; F:ATPase activator activity; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0098655; P:cation transmembrane transport; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; ISO:RGD.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0086009; P:membrane repolarization; ISO:RGD.
DR GO; GO:0030001; P:metal ion transport; IDA:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:RGD.
DR GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; ISO:RGD.
DR GO; GO:1903408; P:positive regulation of P-type sodium:potassium-exchanging transporter activity; ISO:RGD.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:1903169; P:regulation of calcium ion transmembrane transport; ISO:RGD.
DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0055119; P:relaxation of cardiac muscle; ISO:RGD.
DR GO; GO:0001666; P:response to hypoxia; IDA:RGD.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IDA:RGD.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR015565; Na/K_ATPase_sub_beta_chordates.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR PANTHER; PTHR11523:SF10; PTHR11523:SF10; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glutathionylation; Glycoprotein; Immunity; Innate immunity; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Signal-anchor; Sodium; Sodium transport;
KW Sodium/potassium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..304
FT /note="Sodium/potassium-transporting ATPase subunit beta-1"
FT /id="PRO_0000219100"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..62
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 191..304
FT /note="immunoglobulin-like"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14094"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 126..149
FT /evidence="ECO:0000250"
FT DISULFID 159..175
FT /evidence="ECO:0000250"
FT DISULFID 214..277
FT /evidence="ECO:0000250"
FT CONFLICT 183
FT /note="V -> M (in Ref. 2; AAA40780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 304 AA; 35202 MW; 86C3120F463B7B2B CRC64;
MARGKAKEEG SWKKFIWNSE KKEFLGRTGG SWFKILLFYV IFYGCLAGIF IGTIQVMLLT
ISELKPTYQD RVAPPGLTQI PQIQKTEISF RPNDPKSYEA YVLNIIRFLE KYKDSAQKDD
MIFEDCGSMP SEPKERGEFN HERGERKVCR FKLDWLGNCS GLNDESYGYK EGKPCIIIKL
NRVLGFKPKP PKNESLETYP LTMKYNPNVL PVQCTGKRDE DKDKVGNIEY FGMGGFYGFP
LQYYPYYGKL LQPKYLQPLL AVQFTNLTLD TEIRIECKAY GENIGYSEKD RFQGRFDVKI
EVKS
